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Protein

Toluene-4-monooxygenase system protein D

Gene

tmoD

Organism
Pseudomonas mendocina
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Effector protein subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol. Required for optimal efficiency and specificity of the holoenzyme.3 Publications

Pathwayi: toluene degradation

This protein is involved in the pathway toluene degradation, which is part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the pathway toluene degradation and in Xenobiotic degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Enzyme and pathway databases

UniPathwayiUPA00273.

Names & Taxonomyi

Protein namesi
Recommended name:
Toluene-4-monooxygenase system protein D (EC:1.14.13.-)
Alternative name(s):
T4mo effector protein D
Short name:
T4moD
Toluene-4-monooxygenase effector protein
Gene namesi
Name:tmoD
OrganismiPseudomonas mendocina
Taxonomic identifieri300 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000726022 – 103Toluene-4-monooxygenase system protein DAdd BLAST102

Interactioni

Subunit structurei

The multicomponent enzyme toluene-4-monooxygenase is formed by the TmoA, TmoB, TmoC, TmoD, TmoE and TmoF polypeptides. The heterohexamer formed by two molecules each of TmoA, TmoB and TmoE interacts with the effector protein TmoD, the Rieske iron-sulfur protein TmoC and the NADH-containing oxidoreductase TmoF.3 Publications

Protein-protein interaction databases

DIPiDIP-48646N.

Structurei

Secondary structure

1103
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 9Combined sources7
Beta strandi13 – 21Combined sources9
Helixi24 – 34Combined sources11
Beta strandi41 – 44Combined sources4
Beta strandi46 – 60Combined sources15
Helixi61 – 68Combined sources8
Beta strandi70 – 72Combined sources3
Helixi74 – 79Combined sources6
Beta strandi81 – 90Combined sources10
Beta strandi92 – 98Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G10NMR-A2-103[»]
1G11NMR-A2-103[»]
2BF2X-ray2.10A/B2-103[»]
2BF3X-ray1.96A/B12-103[»]
2BF5X-ray1.71A/B6-103[»]
3DHHX-ray1.94E1-103[»]
3DHIX-ray1.68E1-103[»]
3GE3X-ray1.52E1-103[»]
3GE8X-ray2.19E/H1-103[»]
3I5JX-ray1.90E1-103[»]
3I63X-ray2.09E1-103[»]
3Q14X-ray1.75E1-103[»]
3Q2AX-ray1.99E1-103[»]
3Q3MX-ray1.75E/H1-103[»]
3Q3NX-ray1.84E1-103[»]
3Q3OX-ray1.95E1-103[»]
3RI7X-ray2.10E3-103[»]
ProteinModelPortaliQ00459.
SMRiQ00459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00459.

Family & Domainsi

Family and domain databases

Gene3Di3.90.56.10. 1 hit.
InterProiIPR003454. mOase_MmoB_DmpM.
[Graphical view]
PfamiPF02406. MmoB_DmpM. 1 hit.
[Graphical view]
ProDomiPD004249. mOase_MmoB_DmpM. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56029. SSF56029. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLADQALH NNNVGPIIRA GDLVEPVIET AEIDNPGKEI TVEDRRAYVR
60 70 80 90 100
IAAEGELILT RKTLEEQLGR PFNMQELEIN LASFAGQIQA DEDQIRFYFD

KTM
Length:103
Mass (Da):11,618
Last modified:January 23, 2007 - v2
Checksum:i262B14CC1B80644A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65106 Genomic DNA. Translation: AAA26002.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65106 Genomic DNA. Translation: AAA26002.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G10NMR-A2-103[»]
1G11NMR-A2-103[»]
2BF2X-ray2.10A/B2-103[»]
2BF3X-ray1.96A/B12-103[»]
2BF5X-ray1.71A/B6-103[»]
3DHHX-ray1.94E1-103[»]
3DHIX-ray1.68E1-103[»]
3GE3X-ray1.52E1-103[»]
3GE8X-ray2.19E/H1-103[»]
3I5JX-ray1.90E1-103[»]
3I63X-ray2.09E1-103[»]
3Q14X-ray1.75E1-103[»]
3Q2AX-ray1.99E1-103[»]
3Q3MX-ray1.75E/H1-103[»]
3Q3NX-ray1.84E1-103[»]
3Q3OX-ray1.95E1-103[»]
3RI7X-ray2.10E3-103[»]
ProteinModelPortaliQ00459.
SMRiQ00459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48646N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00273.

Miscellaneous databases

EvolutionaryTraceiQ00459.

Family and domain databases

Gene3Di3.90.56.10. 1 hit.
InterProiIPR003454. mOase_MmoB_DmpM.
[Graphical view]
PfamiPF02406. MmoB_DmpM. 1 hit.
[Graphical view]
ProDomiPD004249. mOase_MmoB_DmpM. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56029. SSF56029. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTMOD_PSEME
AccessioniPrimary (citable) accession number: Q00459
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.